Although the conformations of two linked peptide units both with glycyl and alanyl residues have been extensively studied,'-$ no systematic investigation of the energies of conformations of two linked peptide units with side chains beyond the CB atom and a comparison with the available crystallograp
Backbone conformation of amino acids
β Scribed by V. Saisekharan; P. K. Ponnuswamy
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1969
- Tongue
- English
- Weight
- 206 KB
- Volume
- 7
- Category
- Article
- ISSN
- 0006-3525
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The thioredoxin reductase active-site fragment H-Ala-Cys-Ala-Thr-Cys-Asp-Gly-Phe-OH [134 -141], which is known for its high tendency to assume an almost identical conformation as in the intact enzyme, was backbone cyclized with the photoresponsive (4-amino)phenylazobenzoic acid (APB) to produce a mo
## Abstract **A flexible tool for rigid systems**. Residual dipolar couplings (RDCs) have proven to be valuable NMR structural parameters that provide insights into the backbone conformations of short linear peptidic foldamers, as illustrated here. This study demonstrates that RDCs at natural abund